Data di Pubblicazione:
2005
Citazione:
S-nitrosation vs. S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione / D. Giustarini, A.D.G. Milzani, G. Aldini, M. Carini, R. Rossi, I. Dalle-Donne. - In: ANTIOXIDANTS & REDOX SIGNALING. - ISSN 1523-0864. - 7:7-8(2005 Jul), pp. 930-939.
Abstract:
S-Nitrosation of protein sulfhydryl groups is an established response to oxidative/nitrosative stress. The transient nature and reversibility of S-nitrosation, as well as its specificity, render this posttranslational modification an attractive mechanism of regulation of protein function and signal transduction, in analogy to S-glutathionylation. Several feasible mechanisms for protein S-nitrosation have been proposed, including transnitrosation by S-nitrosothiols, such as S-nitrosoglutathione (GSNO), where the nitrosonium moiety is directly transferred from one thiol to another. The reaction between GSNO and protein sulfhydryls can also produce a mixed disulfide by S-glutathionylation, which involves the nucleophilic attack of the sulfur of GSNO by the protein thiolate anion. In this study, we have investigated the possible occurrence of S-glutathionylation during reaction of GSNO with papain, creatine phosphokinase, glyceraldehyde-3-phosphate dehydrogenase, alcohol dehydrogenase, bovine serum albumin, and actin. Our results show that papain, creatine phosphokinase, and glyceraldehyde-3-phosphate dehydrogenase were significantly both S-nitrosated and S-glutathionylated by GSNO, whereas alcohol dehydrogenase, bovine serum albumin, and actin appeared nearly only S-nitrosated. The susceptibility of the modified proteins to denitrosation and deglutathionylation by reduced glutathione was also investigated.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
D. Giustarini, A.D.G. Milzani, G. Aldini, M. Carini, R. Rossi, I. Dalle-Donne
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